Reviewed, UniProtKB/Swiss-Prot P53397 (OGG1_YEAST)

Names and origin

Protein names

Recommended name:
    N-glycosylase/DNA lyase
Including the following 2 domains:
    1- Recommended name:
            8-oxoguanine DNA glycosylase
              EC=3.2.2.-
    2- Recommended name:
            DNA-(apurinic or apyrimidinic site) lyase
                Short name=AP lyase
              EC=4.2.99.18

Gene names

Name:	OGG1
Ordered Locus Names:	YML060W
ORF Names:	YM9958.02

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	376 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	DNA repair enzyme that incises DNA at 8-oxoG residues. Excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine (FAPY) from damaged DNA. Has a beta-lyase activity that nicks DNA 3' to the lesion.
Catalytic activity	The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.
Subcellular location	Nucleus.
Miscellaneous	Present with 3690 molecules/cell in log phase SD medium. Ref.5
Sequence similarities	Belongs to the type-1 OGG1 family.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Nucleus
Molecular function	Glycosidase Hydrolase Lyase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	base-excision repair, AP site formation Ref.1 Inferred from direct assay. Source: SGD nucleotide-excision repair Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrion Inferred from direct assay. Source: SGD nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	damaged DNA binding Inferred from electronic annotation. Source: InterPro oxidized purine base lesion DNA N-glycosylase activity Ref.1 Inferred from direct assay. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 376	376	N-glycosylase/DNA lyase		PRO_0000058595
Sites
	Active site	241	1	Schiff-base intermediate with DNA
	Binding site	134	1	DNA By similarity
	Binding site	139	1	DNA By similarity
	Binding site	189	1	DNA By similarity
	Binding site	258	1	8-oxoguanine; via carbonyl oxygen By similarity
	Binding site	260	1	8-oxoguanine By similarity
	Binding site	262	1	DNA By similarity
	Binding site	320	1	8-oxoguanine By similarity
	Binding site	324	1	8-oxoguanine By similarity
Experimental info
	Mutagenesis	241	1	K → Q: Abolishes both DNA glycosylase and AP lyase activity. Ref.3 Ref.4
	Mutagenesis	241	1	K → R: Diminishes both DNA glycosylase and AP lyase activity. Ref.3 Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P53397-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 4ADB72EB20E4BF20	FASTA	376	42,781
	10 20 30 40 50 60 MSYKFGKLAI NKSELCLANV LQAGQSFRWI WDEKLNQYST TMKIGQQEKY SVVILRQDEE 70 80 90 100 110 120 NEILEFVAVG DCGNQDALKT HLMKYFRLDV SLKHLFDNVW IPSDKAFAKL SPQGIRILAQ 130 140 150 160 170 180 EPWETLISFI CSSNNNISRI TRMCNSLCSN FGNLITTIDG VAYHSFPTSE ELTSRATEAK 190 200 210 220 230 240 LRELGFGYRA KYIIETARKL VNDKAEANIT SDTTYLQSIC KDAQYEDVRE HLMSYNGVGP 250 260 270 280 290 300 KVADCVCLMG LHMDGIVPVD VHVSRIAKRD YQISANKNHL KELRTKYNAL PISRKKINLE 310 320 330 340 350 360 LDHIRLMLFK KWGSYAGWAQ GVLFSKEIGG TSGSTTTGTI KKRKWDMIKE TEAIVTKQMK 370 LKVELSDLHI KEAKID

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression in Escherichia coli of the OGG1 gene of Saccharomyces cerevisiae, which codes for a DNA glycosylase that excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine." van der Kemp P.A., Thomas D., Barbey R., de Oliveira R., Boiteux S. Proc. Natl. Acad. Sci. U.S.A. 93:5197-5202(1996) [PubMed: 8643552] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 28383 / FL100 / VTT C-80102.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. , Skelton J., Walsh S.V., Whitehead S., Barrell B.G. Nature 387:90-93(1997) [PubMed: 9169872] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"The Ogg1 protein of Saccharomyces cerevisiae: a 7,8-dihydro-8-oxoguanine DNA glycosylase/AP lyase whose lysine 241 is a critical residue for catalytic activity." Girard P.-M., Guibourt N., Boiteux S. Nucleic Acids Res. 25:3204-3211(1997) [PubMed: 9241232] [Abstract] Cited for: CHARACTERIZATION, MUTAGENESIS OF LYS-241.
[4]	"Catalytic and DNA binding properties of the ogg1 protein of Saccharomyces cerevisiae: comparison between the wild type and the K241R and K241Q active-site mutant proteins." Guibourt N., Castaing B., Van Der Kemp P.A., Boiteux S. Biochemistry 39:1716-1724(2000) [PubMed: 10677220] [Abstract] Cited for: CHARACTERIZATION, MUTAGENESIS OF LYS-241.
[5]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U44855 Genomic DNA. Translation: AAC49312.1. Z46729 Genomic DNA. Translation: CAA86715.1.
PIR	S49801.
RefSeq	NP_013651.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4538N.
IntAct	P53397. 1 interaction.
STRING	P53397.
Genome annotation databases
Ensembl	YML060W; YML060W; YML060W; Saccharomyces cerevisiae. [Genome view]
GeneID	854942.
KEGG	sce:YML060W.
NMPDR	fig|4932.3.peg.4688.
Organism-specific databases
CYGD	YML060w.
SGD	S000004525. OGG1.
Phylogenomic databases
HOGENOM	HBG551361.
OMA	YAGWAQG.
OrthoDB	EOG9WSXSP.
Enzyme and pathway databases
BRENDA	4.2.99.18. 250.
Gene expression databases
ArrayExpress	P53397.
Genevestigator	P53397.
GermOnline	YML060W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR011257. DNA_glycosylase. IPR003265. HhH-GPD_domain. IPR004577. Ogg. IPR012904. OGG_N. IPR012294. TFIID_C/glycos_N. [Graphical view]
Pfam	PF00730. HhH-GPD. 1 hit. PF07934. OGG_N. 1 hit. [Graphical view]
SMART	SM00478. ENDO3c. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	977995.

Entry information

Entry name

OGG1_YEAST

Accession

Primary (citable) accession number: P53397

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	December 15, 2009
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)